1ir3: Difference between revisions

Revision as of 13:51, 1 July 2008

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File:1ir3.png

Template:STRUCTURE 1ir3

PHOSPHORYLATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOGPHOSPHORYLATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOG

Template:ABSTRACT PUBMED 9312016

About this StructureAbout this Structure

1IR3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog., Hubbard SR, EMBO J. 1997 Sep 15;16(18):5572-81. PMID:9312016

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OCA

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-'''PHOSPHORYLATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOG'''
+===PHOSPHORYLATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOG===
-==Overview==
+<!--
-The crystal structure of the phosphorylated, activated form of the insulin receptor tyrosine kinase in complex with a peptide substrate and an ATP analog has been determined at 1.9 A resolution. The activation loop (A-loop) of the kinase undergoes a major conformational change upon autophosphorylation of Tyr1158, Tyr1162 and Tyr1163 within the loop, resulting in unrestricted access of ATP and protein substrates to the kinase active site. Phosphorylated Tyr1163 (pTyr1163) is the key phosphotyrosine in stabilizing the conformation of the tris-phosphorylated A-loop, whereas pTyr1158 is completely solvent-exposed, suggesting an availability for interaction with downstream signaling proteins. The YMXM-containing peptide substrate binds as a short anti-parallel beta-strand to the C-terminal end of the A-loop, with the methionine side chains occupying two hydrophobic pockets on the C-terminal lobe of the kinase. The structure thus reveals the molecular basis for insulin receptor activation via autophosphorylation, and provides insights into tyrosine kinase substrate specificity and the mechanism of phosphotransfer.
+The line below this paragraph, {{ABSTRACT_PUBMED_9312016}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9312016 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9312016}}
 ==About this Structure==
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 [[Category: Signal transduction]]
 [[Category: Tyrosine kinase]]
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